ArticleMolecules (Basel, Switzerland)2020
Synthesis of the Novel Covalent Cysteine Proteases Inhibitor with Iodoacetic Functional Group.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Reversible Inhibition of Cysteine Proteases Using S-Methyl Methanethiosulfonate.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Comparative proteomic analysis provides new insights into regulation of microspore embryogenesis induction in winter triticale (× Triticosecale Wittm.) after 5-azacytidine treatment.Scientific reports · 2021Article
- Changes in the Flower and Leaf Proteome of Common Buckwheat (International journal of molecular sciences · 2021Article
- New Cysteine Protease Inhibitors: Electrophilic (Het)arenes and Unexpected Prodrug Identification for theMolecules (Basel, Switzerland) · 2020Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
This work presents the synthesis of the novel covalent inhibitor of cysteine proteases where epoxide has been replaced by the iodoacetyl functional group. The molecule, similar in action to E-64 and DCG-04, the commonly applied inhibitors, is additionally biotinylated and contains tyrosyl iodination sites. The Fmoc solid phase synthesis has been applied. Conjugation of iodoacetic acid with the peptide was optimized by testing different conjugation agents. The purity of the final product was verified by mass spectrometry and its bioactivity was tested by incubation with a model cysteine protease-staphopain C. Finally, it was shown that the synthesized inhibitor binds to the protein at the ratio of 1:1. More detailed analysis by means of tandem mass spectrometry proved that the inhibitor binds to the cysteine present in the active site of the enzyme.
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Registered trials
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